Brain capillary guanosine triphosphatase: a distinction from adenosine triphosphatase
- PMID: 6102040
- DOI: 10.1007/BF02003958
Brain capillary guanosine triphosphatase: a distinction from adenosine triphosphatase
Abstract
Differences in kinetic properties, pH response, sensitivity to ouabain, and disc-acrylamide electrophoresis resolution, are observed when GTP and ATP are used as the substrates for triphosphohydrolases in isolated rat brain microvessels. In brain parenchyma there are no such differences. It is concluded that substrate-specific GTPase exists in brain microvessels.
Similar articles
-
Purification and characterization of the major nucleoside triphosphatase from rat liver nuclear envelopes.J Biol Chem. 1986 Jan 15;261(2):663-8. J Biol Chem. 1986. PMID: 2867090
-
Characterisation of Ca2+ or Mg(2+)-dependent nucleoside triphosphatase from rat mesenteric small arteries.Biochim Biophys Acta. 1991 Aug 26;1067(2):191-200. doi: 10.1016/0005-2736(91)90043-8. Biochim Biophys Acta. 1991. PMID: 1652284
-
Guanosine triphosphatase activity in human erythrocyte membranes.Biochim Biophys Acta. 1980 Sep 18;601(2):372-9. doi: 10.1016/0005-2736(80)90541-6. Biochim Biophys Acta. 1980. PMID: 6105884
-
Bioenergetics and kinetics of microtubule and actin filament assembly-disassembly.Int Rev Cytol. 1982;78:1-125. Int Rev Cytol. 1982. PMID: 6128332 Review. No abstract available.
-
Exchange factors, effectors, GAPs and motor proteins: common thermodynamic and kinetic principles for different functions.Eur Biophys J. 2002 Jul;31(4):268-74. doi: 10.1007/s00249-002-0225-3. Epub 2002 Jun 21. Eur Biophys J. 2002. PMID: 12122473 Review.